Analytical Data
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Gene name
YebF
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简介
YebF protein, existing as a monomer in solution, interacts with OmpF/OmpC at the periplasmic face of the membrane, indicating a role in bacterial membrane-related processes. Its monomeric state emphasizes independent structure, prompting further investigation into the molecular mechanisms and functional impact of its interactions with OmpF/OmpC in the bacterial membrane. YebF Protein, E.coli (Myc, His) is the recombinant E. coli-derived YebF protein, expressed by E. coli , with N-His, C-Myc labeled tag.
- Application
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Alternative Names
yebF; b1847; JW1836; Protein YebF
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Species
E.coli
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Source
E. coli
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Tag
N-His;C-Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P33219
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Expression Region
A22-R118
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Protein Length
Full Length of Mature Protein
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
YebF is a relatively understudied protein found in Escherichia coli that has garnered interest due to its potential roles in various cellular processes. As a member of the family of uncharacterized proteins, YebF is thought to participate in stress responses, cellular signaling, and possibly in the regulation of gene expression. Previous studies have indicated that YebF may be implicated in the bacterial adaptation to environmental challenges, such as oxidative stress, thus playing a critical role in bacterial survival and pathogenicity. With the rise in antibiotic resistance, understanding the molecular mechanisms of proteins like YebF becomes increasingly important for developing new therapeutic strategies. Additionally, the recombinant expression of YebF allows for detailed biochemical characterization and functional assays, which can provide insights into its structural properties and interactions with other cellular components. Investigating YebF not only enhances our understanding of bacterial physiology but also could lead to novel approaches for combating bacterial infections. The exploration of YebF’s function and its potential applications in biotechnology and medicine underscores the importance of this protein in the broader context of microbial research.
